ID A0A0V1DD17_TRIBR Unreviewed; 1143 AA.
AC A0A0V1DD17;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=T03_17225 {ECO:0000313|EMBL:KRY59329.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY59329.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY59329.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY59329.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the TOP6A family.
CC {ECO:0000256|ARBA:ARBA00006559}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY59329.1}.
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DR EMBL; JYDI01000013; KRY59329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DD17; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 2.
DR Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KRY59329.1}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:KRY59329.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022645, ECO:0000313|EMBL:KRY59329.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Signal {ECO:0000256|SAM:SignalP};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1143
FT /note="DNA topoisomerase (ATP-hydrolyzing)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876667"
FT DOMAIN 154..176
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 301..311
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 1143 AA; 130587 MW; 45DDC2FD63D92C80 CRC64;
MLQLVSLIFP FFMLITATAD KENYAMQSNA VYKVMRTVPT NESQLKFLQI MYQHADGDQC
KEHNISLRIS IPDVEKFLSE KQTRRSKGRV RRFNYLTTPY FDISVYHSYS EIQNYMRNLE
KQYPHIAKVH TIGYTHENRE INLIQIGRFY SSQPAIWIDA GIHAREWIAP STALYIINYL
VTRYDFDMEV QKYVNGLTWY ILPVVNPDGY EFSRSSLNPR VRLWRKNRSP ANCQPFRNSY
CCRGVDLNRN FDFKWNQQGG SQDPCQETYS GRSAFSEPET QAIERFILQR ADQLGAFVTL
HSYSQIWMYP YGNQRYSYPK DVHDLNTVCC VILDPASGGS EDWAKAVAGI KYSFLVELRP
EEDNQDGFIL DESHIIPTGK ETLEGIKEVA MVLLPGNHNS YFPNTDASSV CQDFHPMCKI
WAVFGACLND TEVRRLCVKS CELCSELDNQ DEKLFIAIGA AESAKDIYGD ADWLPGMEDK
GAFASISRIM SKMKAQSFPL PENSVCQVGN ANLPRTLMWR KGGKAAWLAD PPLTTVGCNT
AKIYAEGLVS ANVLNAQLLG NCVYAAPNFR CVQTADIILK VVDPSGQIKI RIVPELEAES
QVMDKNPCWY IKTDQFSAHN IHRVDVAHKS KKRTKDFSQR KGILDEIQRN HDGNVALFIV
SDWKIKDLCH AICNCKISSE NNAVCENRAI SLLRGRWKYM ECFQAKTDQD LVLRKIEHCI
FAFCLSLFIG PRPALYLPRA KEYALEMTTR NCHMFPIVLC LLSESYSLLR NSQYCTKRNL
YYKHRYLFRS EGDLDRAIKA ICKILVTPRY KLNILSSPKG LVLGDLVLQL GNTEIVDCNS
ISTIPTRSDE FQVLTTSATF ILIVEKDSIF EKLAMEKANS VLRSAILITA KGYPDFPTRL
FLRKLYDYLK LPMFALMDAD PCGIEIFLTY KYGPMNVSYE SGVNVLLPWM KWIGVYPSEI
SSLNLSDTQK LMLGIRERKL IYSLLNRFEA SGDHFLINQL HELNKIGCKV EIEAICSISS
SYLIHEYLKI KRRVEPRERA YGAIAIALVK SYAPTSGEKR NCESNKDLMK SISSVQRGPN
CFDLETLKYL ADLSEVNILA AEAKITTTKT FHENEFDSEK AQLDEIIAIF YGHSIRHSQI
HIN
//
